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Similarities in amino acid sequences, three-dimensional structures, and the exon-intron patterns of their genes have indicated that c-type lysozymes and alpha-lactalbumins are homologous proteins, i.e., descended by divergent evolution from a common ancestor. Like the alpha-lactalbumins, echidna milk, horse milk, and pigeon eggwhite lysozymes all bind Ca(II). Models of their three-dimensional structures, based on their amino acid sequences and the known crystal structures of domestic hen eggwhite and human lysozymes and baboon and human alpha-lactalbumins, have been built. The several structures have been compared and their relationships discussed.


Journal article


J Protein Chem

Publication Date





569 - 584


Amino Acid Sequence, Animals, Binding Sites, Biological Evolution, Calcium, Columbidae, Echidna, Egg Proteins, Horses, Isoenzymes, Lactalbumin, Milk Proteins, Molecular Sequence Data, Muramidase, Protein Conformation